By a News Reporter-Staff News Editor at Biotech Week -- Data detailed on Immunology have been presented. According to news reporting originating in Vienna, Austria, by NewsRx journalists, research stated, "The major turnip (Brassica rapa) pollen allergen, belongs to a family of calcium-binding proteins (i.e., two EF-hand proteins), which occur as highly cross-reactive allergens in pollen of weeds, grasses and trees. In this study, the IgE binding capacity and allergenic activity of three recombinant allergen variants containing mutations in their calcium-binding sites were analyzed in sensitized patients with the aim to identify the most suitable hypoallergenic molecule for specific immunotherapy."
The news reporters obtained a quote from the research from Medical University, "Analysis of the wildtype allergen and the mutants regarding IgE reactivity and activation of basophils in allergic patients indicated that the allergen derivative mutated in both calcium-binding domains had the lowest allergenic activity. Gel filtration and circular dichroism experiments showed that both, the wildtype and the double mutant, occurred as dimers in solution and assumed alpha-helical fold, respectively. However, both fold and thermal stability were considerably reduced in the double mutant. The use of bioinformatic tools for evaluation of the solvent accessibility and charge distribution suggested that the reduced IgE reactivity and different structural properties of the double mutant may be due to a loss of negatively charged amino acids on the surface. Interestingly, immunization of rabbits showed that only the double mutant but not the wildtype allergen induced IgG antibodies which recognized the allergen and blocked binding of allergic patients IgE."
According to the news reporters, the research concluded: "Due to the extensive structural similarity and cross-reactivity between calcium-binding pollen allergens the hypoallergenic double mutant may be useful not only for immunotherapy of turnip pollen allergy, but also for the treatment of allergies to other two EF-hand pollen allergens."
For more information on this research see: Characterization of mutants of a highly cross-reactive calcium-binding protein from Brassica pollen for allergen-specific immunotherapy. Immunobiology, 2013;218(9):1155-1165. Immunobiology can be contacted at: Elsevier Gmbh, Urban & Fischer Verlag, Office Jena, P O Box 100537, 07705 Jena, Germany. (Elsevier - www.elsevier.com; Immunobiology - www.elsevier.com/wps/product/cws_home/701769)
Our news correspondents report that additional information may be obtained by contacting T. Garmatiuk, Medical University of Vienna, Inst Med & Chem Lab Diagnost, Vienna, Austria. Additional authors for this research include I. Swoboda, A. Twardosz-Kropfmuller, F. Dall'Antonia, W. Keller, M.B. Singh, P.L. Bhalla, T. Okada, K. Toriyama, M. Weber, M. Ghannadan, W.R. Sperr, K. Blatt, P. Valent, B. Klein, V. Niederberger, M. Curin, N. Balic and Spitz (see also Immunology).
Keywords for this news article include: Antigens, Vienna, Europe, Austria, Allergens, Immunology
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